Literature DB >> 1599442

Specificity constants in the context of protein engineering of two-substrate enzymes.

P C Engel.   

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Year:  1992        PMID: 1599442      PMCID: PMC1132682          DOI: 10.1042/bj2840604

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


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  2 in total

1.  A single amino acid substitution in lactate dehydrogenase improves the catalytic efficiency with an alternative coenzyme.

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2.  A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework.

Authors:  H M Wilks; K W Hart; R Feeney; C R Dunn; H Muirhead; W N Chia; D A Barstow; T Atkinson; A R Clarke; J J Holbrook
Journal:  Science       Date:  1988-12-16       Impact factor: 47.728

  2 in total
  4 in total

1.  Specificity constants for two-substrate reactions.

Authors:  E A Barnsley
Journal:  Biochem J       Date:  1993-04-01       Impact factor: 3.857

2.  Enzyme specificity in reactions of more than one co-substrate.

Authors:  A Cornish-Bowden
Journal:  Biochem J       Date:  1993-04-01       Impact factor: 3.857

3.  Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.

Authors:  Ruth E Davidson; Christopher J Chesters; James D Reid
Journal:  J Biol Chem       Date:  2009-09-19       Impact factor: 5.157

4.  Arginine Kinases from the Precious Corals Corallium rubrum and Paracorallium japonicum: Presence of Two Distinct Arginine Kinase Gene Lineages in Cnidarians.

Authors:  Tomoka Matsuo; Daichi Yano; Kouji Uda; Nozomu Iwasaki; Tomohiko Suzuki
Journal:  Protein J       Date:  2017-12       Impact factor: 2.371

  4 in total

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